MLCK-A is required for efficient cytokinesis and Con A-induced RLC phosphorylation in Dictyostelium, but the presence of residual RLC phosphorylation in mutants suggests multiple MLCKs exist.
No immediate clinical implications; leaves open MLCK-A's role in mammalian cardiomyocyte cytokinesis.
We have created a strain of Dictyostelium that is deficient for the Ca2+/calmodulin-independent MLCK-A. This strain undergoes cytokinesis less efficiently than wild type, which results in an increased frequency of multinucleate cells when grown in suspension. The MLCK-A-cells are able, however, to undergo development and to cap crosslinked surface receptors, processes that require myosin heavy chain. Phosphorylated regulatory light chain (RLC) is still present in MLCK-A-cells, indicating that Dictyostelium has one or more additional protein kinases capable of phosphorylating RLC. Concanavalin A treatment was found to induce phosphorylation of essentially all of the RLC in wild-type cells, but RLC phosphorylation levels in MLCK-A-cells are unaffected by concanavalin A. Thus MLCK-A is regulated separately from the other MLCK(s) in the cell.
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Smith et al. (1996) studied this question.
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